Research On Interaction Mechanism Of HSA And Some Small Molecule Drugs

Human serum albumin (HSA) is one of the most abundant plasm protein in human body, can combine and transport all kinds of endogenous and exogenous organic compounds, plays an important role for drugs efficacy, often used as a research on protein model of protein-drugs interaction.Most small molecules can combine with human serum albumin, which are transported to the target tissues and organs, which affects drugs metabolism in organism and distribution.Significantly,human serum albumin’s performance not only affect the distribution and effect of some compounds in biological body, but also hinder the pharmaceutical preparations of many potential to reach their targets.In order to study the natural compounds with human serum albumin is how to interact with each other, and to explore the different compounds with the interaction of human serum albumin synergy and inhibition, we decided to explore in the first part of the experiment the interaction of human serum albumin and rhein.In order to achieve the combination of rhein and human serum albumin mechanism and behavior, we through the fluorescence spectroscopy and X-ray crystallography research rhein and the interaction between human serum albumin.Our results reveal that the biochemical and structural characteristics of the interaction, high affinity with low affinity binding sites of the two structure information for guiding the design of new drugs is very meaningful, and for the future development of rhein based compounds and human serum albumin delivery system provides guidance.The second part of the experiment, we manage through fatty acid cis-trans drugs and human serum albumin, to compare the combination of drugs-albumin binding ability, regulation and control of the two drugs in fatty acids.And by cinnamic acid, ribavirin, salicylic acid, indomethacin, shikimic acid ect. with suitable fumaric acid do the competition reaction test, to explore drugs to suitable fumaric acid combined with human serum albumin.The results show that by regulating the function of fatty acids, cis drugs than trans combined with human serum albumin is stronger.For the use of screening drugs for human serum albumin has extremely important significance.And cinnamic acid, ribavirin, salicylic acid, indomethacin, shikimic acid and other drugs of complementation combining ability with human serum albumin,have the influence of different level.In addition, we studied the interaction of xylitol with human serum albumin, and after the use of different concentrations of guanidine hydrochloride in human serum albumin to varying degrees of degeneration, and then investigated the interactions of xylitol and its degeneration after.To explore the xylitol and human serum albumin binding sites, binding constant, and its ability to combine.Studies have suggested that xylitol with HSA in the body can have the effect of storage and transportation, so as to make the xylitol access to their site of action by the circulation of the blood and the efficacy of treatment and health care effect, etc.;In addition, through the xylitol and adding different concentrations of guanidine hydrochloride HSA fluorescence quenching, it can be seen that guanidine hydrochloride as a denaturant, makes the conformation of HSA has changed, the combination of xylitol and HSA constant decreases.This for drug research and development plays an important role, and for understandingthe structure of human serum albumin has very important significance.